scholarly journals Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocket

FEBS Letters ◽  
1989 ◽  
Vol 250 (2) ◽  
pp. 448-452 ◽  
Author(s):  
K.J. Rothschild ◽  
M.S. Braiman ◽  
T. Mogi ◽  
L.J. Stern ◽  
H.G. Khorana
Keyword(s):  
Amino Acids ◽  
Binding Pocket ◽  
Form Part ◽  
Retinal Binding Pocket ◽  
Conserved Amino Acids

scholarly journals Hydrophobic amino acids in the retinal-binding pocket of bacteriorhodopsin.

1993 ◽  
Vol 268 (27) ◽  
pp. 20305-20311
Author(s):  
D.A. Greenhalgh ◽  
D.L. Farrens ◽  
S Subramaniam ◽  
H.G. Khorana
Keyword(s):  
Amino Acids ◽  
Binding Pocket ◽  
Hydrophobic Amino Acids ◽  
Retinal Binding Pocket

Negatively-charged amino acids at the peptide-binding pocket of HLA-DPB1 alleles are associated with susceptibility to anti-topoisomerase I-positive systemic sclerosis

2016 ◽  
Vol 77 (7) ◽  
pp. 550-554 ◽  
Author(s):  
Jeong Seok Lee ◽  
Jin Kyun Park ◽  
Heung Jae Kim ◽  
Hyung Ki Lee ◽  
Yeong Wook Song ◽  
...  
Keyword(s):  
Amino Acids ◽  
Systemic Sclerosis ◽  
Topoisomerase I ◽  
Peptide Binding ◽  
Binding Pocket ◽  
Charged Amino Acids

scholarly journals Molecular cloning and characterization of ornithine decarboxylase cDNA of the nematode Panagrellus redivivus

1995 ◽  
Vol 308 (2) ◽  
pp. 635-640 ◽  
Author(s):  
H von Besser ◽  
G Niemann ◽  
B Domdey ◽  
R D Walter
Keyword(s):  
Amino Acids ◽  
Active Sites ◽  
Cdna Clones ◽  
Degenerate Primers ◽  
Calculated Molecular Mass ◽  
Panagrellus Redivivus ◽  
Free Living Nematode ◽  
Mixed Stage ◽  
Conserved Amino Acids

In a PCR with degenerate primers encoding highly conserved amino acids within ornithine decarboxylases (ODCs) of several organisms, a fragment of the ODC gene of the free-living nematode Panagrellus redivivus was isolated. Northern blot analysis revealed a single 1.7 kb transcript in a mixed-stage population of animals. From this RNA source, a cDNA library was constructed and screened with the PCR fragment. Several cDNA clones were isolated, one of which encodes the complete 435-amino-acid ODC enzyme with a calculated molecular mass of 47.1 kDa. The P. redivivus ODC possesses 126 of the 136 highly conserved amino acids in the enzymes from fungi, invertebrates and vertebrates. Functional amino acids are conserved, suggesting that the two active sites of the P. redivivus ODC are formed at the interface of a homodimer, as described for mammalian ODCs.

scholarly journals Impact of Mutations in Highly Conserved Amino Acids of the HIV-1 Gag-p24 and Env-gp120 Proteins on Viral Replication in Different Genetic Backgrounds

PLoS ONE ◽  
2014 ◽  
Vol 9 (4) ◽  
pp. e94240 ◽  
Author(s):  
Yi Liu ◽  
Ushnal Rao ◽  
Jan McClure ◽  
Philip Konopa ◽  
Siriphan Manocheewa ◽  
...  
Keyword(s):  
Amino Acids ◽  
Viral Replication ◽  
Conserved Amino Acids ◽  
Hiv 1

scholarly journals Reconstruction of the Complete Ouabain-binding Pocket of Na,K-ATPase in Gastric H,K-ATPase by Substitution of Only Seven Amino Acids

2005 ◽  
Vol 280 (37) ◽  
pp. 32349-32355 ◽  
Author(s):  
Li Yan Qiu ◽  
Elmar Krieger ◽  
Gijs Schaftenaar ◽  
Herman G. P. Swarts ◽  
Peter H. G. M. Willems ◽  
...  
Keyword(s):  
Amino Acids ◽  
Binding Pocket ◽  
Ouabain Binding
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